Uracil-DNA glycosylase-like domain superfamily (IPR036895)
Short name: Uracil-DNA_glycosylase-like_sf
- Uracil-DNA glycosylase family 1 (IPR002043)
- G/U mismatch-specific uracil/thymine-DNA glycosylase (IPR003310)
- Uracil-DNA glycosylase-like (IPR005122)
- Uracil-DNA glycosylase family 4 (IPR005273)
- G/U mismatch-specific DNA glycosylase (IPR015637)
- Uracil-DNA glycosylase, active site (IPR018085)
- G/U mismatch-specific DNA glycosylase, bacterial (IPR023502)
- Hypoxanthine-DNA glycosylase (IPR026353)
- Domain of unknown function DUF4918 (IPR032579)
- Single-strand selective monofunctional uracil DNA glycosylase (IPR039134)
This entry represents various uracil-DNA glycosylases and related DNA glycosylases (EC:3.2.2), such as uracil-DNA glycosylase [PMID: 7697717], thermophilic uracil-DNA glycosylase [PMID: 10339434], G:T/U mismatch-specific DNA glycosylase (Mug) [PMID: 9489705], and single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) [PMID: 2820976]. These proteins have a 3-layer alpha/beta/alpha structure.
Uracil-DNA glycosylases are DNA repair enzymes that excise uracil residues from DNA by cleaving the N-glycosylic bond, initiating the base excision repair pathway. Uracil in DNA can arise either through the deamination of cytosine to form mutagenic U:G mispairs, or through the incorporation of dUMP by DNA polymerase to form U:A pairs [PMID: 17116429]. These aberrant uracil residues are genotoxic [PMID: 16860315]. The sequence of uracil-DNA glycosylase is extremely well conserved [PMID: 2555154] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses [PMID: 8389453].